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P42321

- CATA_PROMI

UniProt

P42321 - CATA_PROMI

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Protein

Catalase

Gene

katA

Organism
Proteus mirabilis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Heme group.
NADP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541
Active sitei127 – 1271
Metal bindingi337 – 3371Iron (heme axial ligand)1 Publication

GO - Molecular functioni

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

SABIO-RKP42321.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:katA
OrganismiProteus mirabilis
Taxonomic identifieri584 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484CatalasePRO_0000084992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Methionine sulfone1 Publication

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193
Beta strandi22 – 243
Helixi34 – 4310
Beta strandi52 – 543
Beta strandi56 – 6611
Turni71 – 733
Helixi77 – 793
Beta strandi85 – 939
Beta strandi95 – 973
Beta strandi103 – 1075
Beta strandi110 – 1178
Beta strandi120 – 13011
Helixi137 – 1393
Helixi140 – 1478
Turni151 – 1533
Helixi158 – 1669
Helixi169 – 1713
Helixi172 – 1798
Helixi181 – 1833
Beta strandi184 – 1863
Helixi188 – 1903
Beta strandi199 – 2024
Beta strandi208 – 21710
Helixi226 – 23510
Helixi239 – 24911
Beta strandi255 – 26410
Helixi265 – 2695
Beta strandi271 – 2733
Turni284 – 2863
Beta strandi290 – 29910
Helixi304 – 3074
Turni308 – 3103
Helixi328 – 34518
Helixi349 – 3513
Turni353 – 3553
Beta strandi358 – 3603
Beta strandi382 – 3843
Beta strandi386 – 3883
Helixi394 – 3963
Helixi412 – 4143
Helixi420 – 4289
Helixi431 – 44515
Helixi450 – 46314
Helixi465 – 47814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortaliP42321.
SMRiP42321. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42321.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42321-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE
60 70 80 90 100
RRMHAKGSGA FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG
110 120 130 140 150
AADAERDIRG FALKFYTEEG NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD
160 170 180 190 200
PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS DRGLPLSYRF VHGFGSHTYS
210 220 230 240 250
FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS QRDLFEAIER
260 270 280 290 300
GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN
310 320 330 340 350
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH
360 370 380 390 400
QIPVNAPKCP FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP
410 420 430 440 450
LSIEGAADHW NHREDEDYFS QPRALYELLS DDEHQRMFAR IAGELSQASK
460 470 480
ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG KDAK
Length:484
Mass (Da):55,614
Last modified:November 1, 1995 - v1
Checksum:iADC25F3CB41F5C50
GO

Mass spectrometryi

Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. 1 Publication

Sequence databases

PIRiA58663.

Cross-referencesi

Sequence databases

PIRi A58663.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E93 X-ray 2.00 A 1-484 [» ]
1H6N X-ray 2.11 A 1-484 [» ]
1H7K X-ray 2.40 A 2-484 [» ]
1M85 X-ray 2.00 A 1-484 [» ]
1MQF X-ray 2.50 A 1-484 [» ]
1NM0 X-ray 2.30 A 1-484 [» ]
2CAG X-ray 2.70 A 1-484 [» ]
2CAH X-ray 2.70 A 1-484 [» ]
3HB6 X-ray 2.30 A 1-484 [» ]
ProteinModelPortali P42321.
SMRi P42321. Positions 4-479.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P42321.

Miscellaneous databases

EvolutionaryTracei P42321.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site."
    Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G.
    J. Protein Chem. 14:59-72(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, OXIDATION AT MET-53, MASS SPECTROMETRY.
    Strain: PR.
  2. "Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH."
    Gouet P., Jouve H.-M., Dideberg O.
    J. Mol. Biol. 249:933-954(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: PR.
  3. "Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy."
    Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J.
    Nat. Struct. Biol. 3:951-956(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ABSORPTION SPECTROSCOPY.
  4. "High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron."
    Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.
    Proteins 50:261-271(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), EPR SPECTROSCOPY.

Entry informationi

Entry nameiCATA_PROMI
AccessioniPrimary (citable) accession number: P42321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3